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Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9
Avital-Shmilovici, M., Mandal, K., Gates, Z. P., Phillips, N. B., Weiss, M. A., and Kent, S. B. H. (2013) Fully convergent chemical synthesis of ester insulin: determination of the high resolution X-ray structure by racemic protein crystallography. J Am Chem Soc. 135, 3173-85
Ausin, I., Greenberg, M. V. C., Simanshu, D. K., Hale, C. J., Vashisht, A. A., Simon, S. A., Lee, T. -fen, Feng, S., Española, S. D., Meyers, B. C., Wohlschlegel, J. A., Patel, D. J., and Jacobsen, S. E. (2012) INVOLVED IN DE NOVO 2-containing complex involved in RNA-directed DNA methylation in Arabidopsis. Proc Natl Acad Sci U S A. 109, 8374-81
Atkison, J. H., Parnham, S., Marcotte, W. R., and Olsen, S. K. (2016) Crystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer Interface. J Biol Chem. 291, 19006-17
Atapattu, L., Saha, N., Chheang, C., Eissman, M. F., Xu, K., Vail, M. E., Hii, L., Llerena, C., Liu, Z., Horvay, K., Abud, H. E., Kusebauch, U., Moritz, R. L., Ding, B. - S., Cao, Z., Rafii, S., Ernst, M., Scott, A. M., Nikolov, D. B., Lackmann, M., and Janes, P. W. (2016) An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth. J Exp Med. 213, 1741-57
Assadieskandar, A., Yu, C., Maisonneuve, P., Kurinov, I., Sicheri, F., and Zhang, C. (2019) Rigidification Dramatically Improves Inhibitor Selectivity for RAF Kinases. ACS Med Chem Lett. 10, 1074-1080
Assadieskandar, A., Yu, C., Maisonneuve, P., Liu, X., Chen, Y. - C., Prakash, G. K. Surya, Kurinov, I., Sicheri, F., and Zhang, C. (2018) Effects of rigidity on the selectivity of protein kinase inhibitors. Eur J Med Chem. 146, 519-528
Artavanis-Tsakonas, K., Weihofen, W. A., Antos, J. M., Coleman, B. I., Comeaux, C. A., Duraisingh, M. T., Gaudet, R., and Ploegh, H. L. (2010) Characterization and structural studies of the Plasmodium falciparum ubiquitin and Nedd8 hydrolase UCHL3. J Biol Chem. 285, 6857-66
Arora, K., and Corbett, K. D. (2018) The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding. Nucleic Acids Res. 10.1093/nar/gky1273
Arnett, K. L., Hass, M., McArthur, D. G., Ilagan, M. Xenia G., Aster, J. C., Kopan, R., and Blacklow, S. C. (2010) Structural and mechanistic insights into cooperative assembly of dimeric Notch transcription complexes. Nat Struct Mol Biol. 17, 1312-7
Arndt, J. W., Schwarzenbacher, R., Page, R., Abdubek, P., Ambing, E., Biorac, T., Canaves, J. M., Chiu, H. - J., Dai, X., Deacon, A. M., DiDonato, M., Elsliger, M. - A., Godzik, A., Grittini, C., Grzechnik, S. K., Hale, J., Hampton, E., Han, G. Won, Haugen, J., Hornsby, M., Klock, H. E., Koesema, E., Kreusch, A., Kuhn, P., Jaroszewski, L., Lesley, S. A., Levin, I., McMullan, D., McPhillips, T. M., Miller, M. D., Morse, A., Moy, K., Nigoghossian, E., Ouyang, J., Peti, W. S., Quijano, K., Reyes, R., Sims, E., Spraggon, G., Stevens, R. C., van den Bedem, H., Velasquez, J., Vincent, J., von Delft, F., Wang, X., West, B., White, A., Wolf, G., Xu, Q., Zagnitko, O., Hodgson, K. O., Wooley, J., and Wilson, I. A. (2005) Crystal structure of an alpha/beta serine hydrolase (YDR428C) from Saccharomyces cerevisiae at 1.85 A resolution. Proteins. 58, 755-8
Armstrong, A. A., Mohideen, F., and Lima, C. D. (2012) Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2. Nature. 483, 59-63
Armache, K. - J., Garlick, J. D., Canzio, D., Narlikar, G. J., and Kingston, R. E. (2011) Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.. Science. 334, 977-82
Ardiccioni, C., Clarke, O. B., Tomasek, D., Issa, H. A., von Alpen, D. C., Pond, H. L., Banerjee, S., Rajashankar, K. R., Liu, Q., Guan, Z., Li, C., Kloss, B., Bruni, R., Kloppmann, E., Rost, B., M Manzini, C., Shapiro, L., and Mancia, F. (2016) Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB and insights into the mechanism of catalysis. Nat Commun. 7, 10175
Archer, C. R., Enslow, B. T., Taylor, A. B., De la Rosa, V., Bhattacharya, A., and Shapiro, M. S. (2019) A mutually-induced conformational fit underlies Ca-directed interactions between calmodulin and the proximal C terminus of KCNQ4 K channels. J Biol Chem. 10.1074/jbc.RA118.006857
Arbing, M. A., Kaufmann, M., Phan, T., Chan, S., Cascio, D., and Eisenberg, D. (2010) The crystal structure of the Mycobacterium tuberculosis Rv3019c-Rv3020c ESX complex reveals a domain-swapped heterotetramer. Protein Sci. 19, 1692-703
Arbing, M. A., Chan, S., Harris, L., Kuo, E., Zhou, T. T., Ahn, C. J., Nguyen, L., He, Q., Lu, J., Menchavez, P. T., Shin, A., Holton, T., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2013) Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions. PLoS One. 8, e81753
Arbing, M. A., Chan, S., Shin, A., Phan, T., Ahn, C. J., Rohlin, L., and Gunsalus, R. P. (2012) Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans. Proc Natl Acad Sci U S A. 109, 11812-7
Arbing, M. A., Handelman, S. K., Kuzin, A. P., Verdon, G., Wang, C., Su, M., Rothenbacher, F. P., Abashidze, M., Liu, M., Hurley, J. M., Xiao, R., Acton, T., Inouye, M., Montelione, G. T., Woychik, N. A., and Hunt, J. F. (2010) Crystal structures of Phd-Doc, HigA, and YeeU establish multiple evolutionary links between microbial growth-regulating toxin-antitoxin systems. Structure. 18, 996-1010
Araya-Secchi, R., Neel, B. L., and Sotomayor, M. (2016) An elastic element in the protocadherin-15 tip link of the inner ear. Nat Commun. 7, 13458
Aranda, R., Cai, H., Worley, C. E., Levin, E. J., Li, R., Olson, J. S., Phillips, G. N., and Richards, M. P. (2009) Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins. 75, 217-30
Araghi, R. Rezaei, Bird, G. H., Ryan, J. A., Jenson, J. M., Godes, M., Pritz, J. R., Grant, R. A., Letai, A., Walensky, L. D., and Keating, A. E. (2018) Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells. Proc Natl Acad Sci U S A. 115, E886-E895
Aquino, B., Couñago, R. M., Verza, N., Ferreira, L. M., Massirer, K. B., Gileadi, O., and Arruda, P. (2017) Structural Characterization of Maize SIRK1 Kinase Domain Reveals an Unusual Architecture of the Activation Segment. Front Plant Sci. 8, 852
Apostol, M. I., Perry, K., and Surewicz, W. K. (2013) Crystal structure of a human prion protein fragment reveals a motif for oligomer formation. J Am Chem Soc. 135, 10202-5
Apostol, M. I., Sawaya, M. R., Cascio, D., and Eisenberg, D. (2010) Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease. J Biol Chem. 285, 29671-5